Linked Life Data

9283974

Source:http://linkedlifedata.com/resource/pubmed/id/9283974

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-10-16
pubmed:abstractText
Several sets of atomic solvation parameters imitating: (i) nonpolar environment of hydrocarbon core of a membrane, (ii) aqueous solution, and (iii) weakly-polar solvents have been developed. The parameters have been incorporated into the ECEPP/2 and CHARMM force fields and employed in non-restrained Monte Carlo and molecular dynamics simulations of membrane-spanning alpha-helical peptides (segment A of bacteriorhodopsin, melittin). Through these simulations, the structure and energetics of the helices have been examined as a function of the solvation term in the potential energy function. For the peptides under study, the set (i) of atomic solvation parameters reveals good retention of the alpha-helical conformation. By contrast, the simulations in vacuum or with the parameters imitating a polar solvent (sets (ii) or (iii)) show fast helix destabilization and tight packing of the structure accompanied by significant decreasing of the surface area accessible to solvent. Increased helical propensity for amino acid residues, population of side-chain rotamers as well as hydrogen-bonding pattern in nonpolar membrane-like environment agree well with available experimental and computational data. The problems related to further applications of the membrane-mimicking sets of atomic solvation parameters to simulations of membrane proteins and peptides are addressed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0739-1102
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-18
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Atomic solvation parameters for proteins in a membrane environment. Application to transmembrane alpha-helices.
pubmed:affiliation
Université des Sciences et Technologies de Lille, Centre de Recherches et d'Etudes en Simulations et Modélisation Moléculaires (CRESIMM), Villeneuve d'Ascq, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't